6VUZ
Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT353
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0008080 | molecular_function | N-acetyltransferase activity |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0030649 | biological_process | aminoglycoside antibiotic catabolic process |
A | 0033661 | biological_process | effector-mediated defense to host-produced reactive oxygen species |
A | 0034054 | biological_process | symbiont-mediated suppression of host defense-related programmed cell death |
A | 0034069 | molecular_function | aminoglycoside N-acetyltransferase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0043655 | cellular_component | host extracellular space |
A | 0044161 | cellular_component | host cell cytoplasmic vesicle |
A | 0046677 | biological_process | response to antibiotic |
A | 0051701 | biological_process | biological process involved in interaction with host |
A | 0052032 | biological_process | symbiont-mediated perturbation of host inflammatory response |
A | 0052040 | biological_process | symbiont-mediated perturbation of host programmed cell death |
A | 0052167 | biological_process | symbiont-mediated perturbation of host innate immune response |
A | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
A | 0097691 | cellular_component | bacterial extracellular vesicle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue RMS A 501 |
Chain | Residue |
A | ASP26 |
A | PHE402 |
A | SO4506 |
A | ILE28 |
A | ALA33 |
A | TRP36 |
A | MET65 |
A | SER83 |
A | PHE84 |
A | HIS119 |
A | GLU401 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PEG A 502 |
Chain | Residue |
A | PRO41 |
A | ASP66 |
A | SER111 |
A | TYR113 |
A | PRO342 |
A | THR343 |
A | ASP344 |
A | HOH621 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ARG93 |
A | ARG94 |
A | GLY95 |
A | LEU96 |
A | LEU97 |
A | HOH601 |
A | HOH698 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | PRO72 |
A | GLY73 |
A | ALA391 |
A | SER392 |
A | ASP393 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue PEG A 505 |
Chain | Residue |
A | LEU241 |
A | ILE268 |
A | THR269 |
A | HIS270 |
A | PRO274 |
A | GLN397 |
A | HOH615 |
A | HOH642 |
A | HOH678 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 506 |
Chain | Residue |
A | PHE24 |
A | ASP26 |
A | PHE402 |
A | RMS501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21628583 |
Chain | Residue | Details |
A | TYR126 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor; via carboxylate => ECO:0000305|PubMed:21628583 |
Chain | Residue | Details |
A | PHE402 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0007744|PDB:3RYO |
Chain | Residue | Details |
A | VAL85 | |
A | SER121 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22547814, ECO:0000305|PubMed:21628583, ECO:0000305|PubMed:24106131, ECO:0000305|PubMed:27010218, ECO:0007744|PDB:3RYO |
Chain | Residue | Details |
A | ARG93 |